Evidence map›Paper›PMID 41009482›Full record

ArticleInternational journal of molecular sciences2025

Exploring the Antimicrobial and Antiviral Properties of Cryptic Peptides from Human Fibrinogen.

Andrea Bosso, Antonio Masino, Ilaria Di Nardo, Carla Zannella, Rosa Gaglione, Ida Palumbo, Rosanna Culurciello, Anna De Filippis, Marcelo D T Torres, Cesar de la Fuente-Nunez and 6 more

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Andrea BossoDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0003-2360-300X
Antonio MasinoDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0002-2758-8217
Ilaria Di NardoDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0003-3677-4801
Carla ZannellaDepartment of Experimental Medicine, University of Campania "Luigi Vanvitelli", 80138 Napoli, Italy.ORCID 0000-0001-7991-8700
Rosa GaglioneDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0003-2391-0237
Ida PalumboDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0009-0004-0450-0616
Rosanna CulurcielloDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0002-7083-2908
Anna De FilippisDepartment of Experimental Medicine, University of Campania "Luigi Vanvitelli", 80138 Napoli, Italy.ORCID 0000-0002-0395-7962
Marcelo D T TorresMachine Biology Group, Departments of Psychiatry and Microbiology, Institute for Biomedical Informatics, Institute for Translational Medicine and Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0002-6165-9138
Cesar de la Fuente-NunezMachine Biology Group, Departments of Psychiatry and Microbiology, Institute for Biomedical Informatics, Institute for Translational Medicine and Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0002-2005-5629
Massimiliano GaldieroDepartment of Experimental Medicine, University of Campania "Luigi Vanvitelli", 80138 Napoli, Italy.ORCID 0000-0002-1576-6290
Angela ArcielloDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0001-8269-6459
Antimo Di MaroDepartment of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.ORCID 0000-0002-9595-9665
Elio PizzoDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0002-3652-8865
Valeria CafaroDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0002-6686-7657
Eugenio NotomistaDepartment of Biology, University of Naples Federico II, Via Vicinale Cupa Cintia, 26, 80126 Naples, Italy.ORCID 0000-0003-0097-6487

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrinogen (FIB), a key component of the coagulation cascade, is traditionally recognized for its role in hemostasis and tissue repair. However, due to its high plasma abundance and susceptibility to proteolytic cleavage during inflammation, it may also represent a previously unrecognized source of bioactive peptides. This study presents, for the first time, a comprehensive analysis of the antimicrobial, anti-inflammatory, and antiviral properties of six cationic antimicrobial peptides (AMPs) deriving from the C-terminal extremities of the three subunits of human fibrinogen (FIBα, FIBβ, and FIBγ), identified using a scoring function developed by our group. Antibacterial assays against Gram-positive and Gram-negative pathogens revealed different antimicrobial activity profile depending on their parent protein. Selected peptides displayed additive or synergistic effects when combined with conventional antibiotics or the thrombin-derived peptide (P)GKY20, highlighting their potential for combination therapies. Hemolytic assay confirmed the biocompatibility of fibrinogen-derived cryptic peptides with erythrocytes. Furthermore, the peptides significantly reduced LPS-induced nitric oxide release in murine macrophages Raw 264.7 cells, indicating anti-inflammatory activity. Notably, antiviral activity was observed against enveloped viruses (HCoV-229E and HSV-1) under various treatment conditions, while no activity was detected against the non-enveloped virus CVB3. Overall, these findings reveal human fibrinogen as a source of multifunctional cryptic peptides with broad-spectrum antimicrobial, antiviral, and immunomodulatory activities, supporting their potential as part of the innate immune system.

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesAntiviral AgentsFibrinogenAnimalsAnti-Inflammatory AgentsHemolysisHumansMacrophagesMiceMicrobial Sensitivity TestsNitric OxideRAW 264.7 CellsAnti-Infective AgentsAnti-Inflammatory AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesAntiviral AgentsFibrinogenNitric Oxideanti-biofilmantimicrobial peptidesanti-viral activitycryptic peptidesfibrinogenhost defense peptidesLPS-inhibitionthrombin

Identifiers

PMID41009482
PMCPMC12469503

What Socratic holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.